Catalysis by Micelles, Membranes and other Aqueous Aggregates as Models of Enzyme Action

Toyoki Kunitake, Seiji Shinkai

Research output: Contribution to journalArticlepeer-review

117 Citations (Scopus)


Many biochemical processes proceed in a microheterogeneous system containing organic and aqueous phases. This chapter discusses the structure of various aqueous aggregates. The catalytic action of these aggregates is presented in relation to enzyme catalysis. The underlying theme is the hydrophobic effect. The active site of enzymes is mostly located in a hydrophobic region. Thus, the attachment of enzyme-related functional groups to the hydrophobic core of micelles provides interesting enzyme-model systems. A variety of catalytic groups such as imidazoles and thiols can be enormously activated in a hydrophobic microenvironment. A similar situation exists for coenzyme catalysis. An important area of progress is the enlargement of the scope of the structure of aqueous aggregates. This is highlighted in the chapter.

Original languageEnglish
Pages (from-to)435-487
Number of pages53
JournalAdvances in Physical Organic Chemistry
Issue numberC
Publication statusPublished - Jan 1 1980
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry
  • Organic Chemistry


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